ArticlePloS one2015
Structural Basis Underlying the Binding Preference of Human Galectins-1, -3 and -7 for Galβ1-3/4GlcNAc.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Developing Galectin-3-Targeted Therapeutics in Diseases: Three Distinct Galectin-3 Segments for Targeting.Expert reviews in molecular medicine · 2026Review
- Structural insights into glycan recognition by plant immune receptors: a comparative perspective with animal innate immune systems.The Plant journal : for cell and molecular biology · 2026Review
- Expression and Characterization of Blood Group Binding Lectins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- Galectin-12 in the Regulation of Sebocyte Proliferation, Lipid Metabolism, and Immune Responses.Biomolecules · 2025Review
- Binding free energy analysis of galectin-3 natural ligands and synthetic inhibitors.Protein science : a publication of the Protein Society · 2025Article
- Exploring galectin interactions with human milk oligosaccharides and blood group antigens identifies BGA6 as a functional galectin-4 ligand.The Journal of biological chemistry · 2024Article
- Intracellular galectin interactions in health and disease.Seminars in immunopathology · 2024Review
- Bacterial surface display of human lectins in Escherichia coli.Microbial biotechnology · 2024Article
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- Characterization of Galectin Fusion Proteins with Glycoprotein Affinity Columns and Binding Assays.Molecules (Basel, Switzerland) · 2023Article
- A brief history of galectin evolution.Frontiers in immunology · 2023Article
- Innate immune Galectin-7 specifically targets microbes that decorate themselves in blood group-like antigens.iScience · 2022Article
- Purification of Recombinant Galectins from Different Species Using Distinct Affinity Chromatography Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Functions and Inhibition of Galectin-7, an Emerging Target in Cellular Pathophysiology.Biomolecules · 2021Review
- Degraded Arabinogalactans and Their Binding Properties to Cancer-Associated Human Galectins.International journal of molecular sciences · 2021Article
- Introducing affinity and selectivity into galectin-targeting nanoparticles with fluorinated glycan ligands.Chemical science · 2020Article
- Protective role of Galectin-7 for skin barrier impairment in atopic dermatitis.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2020Article
- Synthesis of the Thomsen-Friedenreich-antigen (TF-antigen) and binding of Galectin-3 to TF-antigen presenting neo-glycoproteins.Glycoconjugate journal · 2020Article
- Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Galectins represent β-galactoside-binding proteins and are known to bind Galβ1-3/4GlcNAc disaccharides (abbreviated as LN1 and LN2, respectively). Despite high sequence and structural homology shared by the carbohydrate recognition domain (CRD) of all galectin members, how each galectin displays different sugar-binding specificity still remains ambiguous. Herein we provided the first structural evidence of human galectins-1, 3-CRD and 7 in complex with LN1. Galectins-1 and 3 were shown to have higher affinity for LN2 than for LN1, while galectin-7 displayed the reversed specificity. In comparison with the previous LN2-complexed structures, the results indicated that the average glycosidic torsion angle of galectin-bound LN1 (ψ(LN1) ≈ 135°) was significantly differed from that of galectin-bound LN2 (ψ(LN2 )≈ -108°), i.e. the GlcNAc moiety adopted a different orientation to maintain essential interactions. Furthermore, we also identified an Arg-Asp/Glu-Glu-Arg salt-bridge network and the corresponding loop (to position the second Asp/Glu residue) critical for the LN1/2-binding preference.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.